Actin polymerization dynamics regulated by actin-binding proteins are essential for various cellular functions. The cofilin family of proteins are potent regulators of actin severing and filament disassembly. The structural basis for cofilin-isoform-specific severing activity is poorly understood as their high-resolution structures in complex with filamentous actin (F-actin) are lacking. Here, we present the atomic-resolution structure of the muscle-tissue-specific isoform, cofilin-2 (CFL2),...
[NMR paper] Structural Analysis of Human Cofilin 2/Filamentous Actin Assemblies: Atomic-Resolution Insights from Magic Angle Spinning NMR Spectroscopy.
Structural Analysis of Human Cofilin 2/Filamentous Actin Assemblies: Atomic-Resolution Insights from Magic Angle Spinning NMR Spectroscopy.
Related Articles Structural Analysis of Human Cofilin 2/Filamentous Actin Assemblies: Atomic-Resolution Insights from Magic Angle Spinning NMR Spectroscopy.
Sci Rep. 2017 Mar 17;7:44506
Authors: Yehl J, Kudryashova E, Reisler E, Kudryashov D, Polenova T
Abstract
Cellular actin dynamics is an essential element of numerous cellular processes, such as cell motility, cell division and...
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03-19-2017 10:38 PM
Studyingthe Conformation of a Silaffin-Derived PentalysinePeptide Embedded in Bioinspired Silica using Solution and DynamicNuclear Polarization Magic-Angle Spinning NMR
Studyingthe Conformation of a Silaffin-Derived PentalysinePeptide Embedded in Bioinspired Silica using Solution and DynamicNuclear Polarization Magic-Angle Spinning NMR
Yasmin Geiger, Hugo E. Gottlieb, U?mit Akbey, Hartmut Oschkinat and Gil Goobes
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.5b07809/20160419/images/medium/ja-2015-07809a_0001.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.5b07809
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/T8sbiifgCd8
[NMR paper] Magic Angle Spinning NMR Reveals Sequence-Dependent Structural Plasticity, Dynamics, and the Spacer Peptide 1 Conformation in HIV-1 Capsid Protein Assemblies.
Magic Angle Spinning NMR Reveals Sequence-Dependent Structural Plasticity, Dynamics, and the Spacer Peptide 1 Conformation in HIV-1 Capsid Protein Assemblies.
Magic Angle Spinning NMR Reveals Sequence-Dependent Structural Plasticity, Dynamics, and the Spacer Peptide 1 Conformation in HIV-1 Capsid Protein Assemblies.
J Am Chem Soc. 2013 Oct 28;
Authors: Han Y, Hou G, Suiter CL, Ahn J, Byeon IJ, Lipton AS, Burton SD, Hung I, Gor'kov PL, Gan Z, Brey WW, Rice D, Gronenborn AM, Polenova TE
Abstract
A key stage in HIV-1 maturation towards...
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10-30-2013 10:44 AM
[NMR paper] Full-length Vpu and human CD4(372-433) in phospholipid bilayers as seen by magic angle spinning NMR.
Full-length Vpu and human CD4(372-433) in phospholipid bilayers as seen by magic angle spinning NMR.
Related Articles Full-length Vpu and human CD4(372-433) in phospholipid bilayers as seen by magic angle spinning NMR.
Biol Chem. 2013 Jul 17;
Authors: Do HQ, Wittlich M, Glück JM, Möckel L, Willbold D, Koenig BW, Heise H
Abstract
Abstract HIV-1 Vpu and CD4(372-433), a peptide comprising the transmembrane and cytoplasmic domain of human CD4, were recombinantly expressed in Escherichia coli, uniformly labeled with 13C und 15N isotopes,...
Magic angle spinning NMR structure of human cofilin-2 assembled on actin filaments reveals isoform-specific conformation and binding mode
Linear Mode
